Enveloped RNA virus utilization of phosphatidylserine receptors: Advantages of exploiting a conserved, widely available mechanism of entry
Fig 1
The TIM-1 PS binding pocket is highly conserved across a wide range of mammalian genomes.
(A) TIM-1 amino acid sequences from NCBI were accessed for human, Egyptian fruit bat, greater horseshoe bat, African green monkey, and house mouse and aligned using CLUSTAL Ω. A region of 30 residues is shown here, encompassing the IgV binding pocket. Highlighted residues have complete identity across all species examined, ▽ depict residues that, if mutated (to alanine), decrease EBOV pseudovirion transduction >20%, and ▲ indicates residues that, if mutated, decrease EBOV GP-rVSV infection >20% according to Moller-Tank and colleagues [45]. (B) Alignment of TIM-4 amino acid sequence to TIM-1 as above. Highlighted residues have identity to all TIM-1 sequences shown, and ▲ indicates residues that, if mutated, significantly reduce transduction and infection according to Rhein and colleagues [30]. EBOV GP-rVSV, Ebola virus glycoprotein-recombinant vesicular stomatitis virus; IgV, immunoglobulin V; PS, phosphatidylserine.